ID A0A1G9YTF1_9EURY Unreviewed; 361 AA.
AC A0A1G9YTF1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000256|HAMAP-Rule:MF_01609};
DE EC=6.3.2.2 {ECO:0000256|HAMAP-Rule:MF_01609};
DE AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000256|HAMAP-Rule:MF_01609};
DE Short=GCS {ECO:0000256|HAMAP-Rule:MF_01609};
DE Short=Gamma-GCS {ECO:0000256|HAMAP-Rule:MF_01609};
GN Name=gshA {ECO:0000256|HAMAP-Rule:MF_01609};
GN ORFNames=SAMN05192554_11620 {ECO:0000313|EMBL:SDN12438.1};
OS Haloarchaeobius iranensis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halorubellaceae; Haloarchaeobius.
OX NCBI_TaxID=996166 {ECO:0000313|EMBL:SDN12438.1, ECO:0000313|Proteomes:UP000199370};
RN [1] {ECO:0000313|EMBL:SDN12438.1, ECO:0000313|Proteomes:UP000199370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB21,IBRC-M 10013,KCTC 4048
RC {ECO:0000313|Proteomes:UP000199370};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC),
CC the main low-molecular-weight thiol compound instead of glutathione in
CC halophilic archaea. {ECO:0000256|HAMAP-Rule:MF_01609}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01609};
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC YbdK subfamily. {ECO:0000256|HAMAP-Rule:MF_01609}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNIA01000016; SDN12438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9YTF1; -.
DR STRING; 996166.SAMN05192554_11620; -.
DR OrthoDB; 287652at2157; -.
DR Proteomes; UP000199370; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.590.20; -; 1.
DR HAMAP; MF_01609; Glu_cys_ligase_2; 1.
DR InterPro; IPR006336; GCS2.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR011793; YbdK.
DR NCBIfam; TIGR02050; gshA_cyan_rel; 1.
DR PANTHER; PTHR36510; GLUTAMATE--CYSTEINE LIGASE 2-RELATED; 1.
DR PANTHER; PTHR36510:SF1; GLUTAMATE--CYSTEINE LIGASE 2-RELATED; 1.
DR Pfam; PF04107; GCS2; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01609, ECO:0000313|EMBL:SDN12438.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01609};
KW Reference proteome {ECO:0000313|Proteomes:UP000199370}.
SQ SEQUENCE 361 AA; 40335 MW; 24938BDCE810F72A CRC64;
MERGSPDAFA EQGTLGVEEE FFVVDEAGYP VSGSDELVYE GERPARLADR LDHELFKTVI
ETQTPKSESL AAARENVHAV REALVEYAAE HGFRVAAAGL HPAARWRELE HAEKDRYRAQ
LERIQYPQHR NTTAGLHVHV GVDDPDKAVW VSNRLRWHLP VMLALSANSP YWNGYDTGLA
SARAKIFEGL PNTGMPTAFA DYEAYQRFEN RMIDSGSIND RGELWHDVRP HSGHGTVEVR
TPDAQADPAV VLAFVEYTEA LVTDLSERYE DLAAPDGTDG CMRREVLDEN KWRALRYGHA
ASFVEREGTG TVDLGEVVDR ECDRLGVSGI RDVYDADSGA TRQRRVLESE GLDALCRELL
V
//
